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Zinc in PDB 1b4t: H48C Yeast Cu(II)/Zn Superoxide Dismutase Room Temperature (298K) Structure

Enzymatic activity of H48C Yeast Cu(II)/Zn Superoxide Dismutase Room Temperature (298K) Structure

All present enzymatic activity of H48C Yeast Cu(II)/Zn Superoxide Dismutase Room Temperature (298K) Structure:
1.15.1.1;

Protein crystallography data

The structure of H48C Yeast Cu(II)/Zn Superoxide Dismutase Room Temperature (298K) Structure, PDB code: 1b4t was solved by P.J.Hart, M.M.Balbirnie, N.L.Ogihara, A.M.Nersissian, M.S.Weiss, J.S.Valentine, D.Eisenberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.80
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 118.647, 118.647, 75.376, 90.00, 90.00, 120.00
R / Rfree (%) 20.9 / 25.8

Other elements in 1b4t:

The structure of H48C Yeast Cu(II)/Zn Superoxide Dismutase Room Temperature (298K) Structure also contains other interesting chemical elements:

Copper (Cu) 1 atom
Chlorine (Cl) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the H48C Yeast Cu(II)/Zn Superoxide Dismutase Room Temperature (298K) Structure (pdb code 1b4t). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the H48C Yeast Cu(II)/Zn Superoxide Dismutase Room Temperature (298K) Structure, PDB code: 1b4t:

Zinc binding site 1 out of 1 in 1b4t

Go back to Zinc Binding Sites List in 1b4t
Zinc binding site 1 out of 1 in the H48C Yeast Cu(II)/Zn Superoxide Dismutase Room Temperature (298K) Structure


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of H48C Yeast Cu(II)/Zn Superoxide Dismutase Room Temperature (298K) Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn155

b:20.1
occ:1.00
 ND1 A:HIS63 2.0 18.7 1.0
OD1 A:ASP83 2.0 20.5 1.0
ND1 A:HIS80 2.1 19.1 1.0
ND1 A:HIS71 2.1 18.0 1.0
CG A:ASP83 2.9 19.4 1.0
CE1 A:HIS63 2.9 18.8 1.0
CE1 A:HIS71 2.9 18.7 1.0
OD2 A:ASP83 3.0 19.8 1.0
CE1 A:HIS80 3.0 18.8 1.0
CG A:HIS63 3.0 16.5 1.0
CG A:HIS80 3.1 18.4 1.0
CG A:HIS71 3.2 17.9 1.0
CB A:HIS63 3.4 14.8 1.0
CB A:HIS80 3.5 17.8 1.0
O A:LYS136 3.6 23.3 1.0
CB A:HIS71 3.6 19.1 1.0
NE2 A:HIS63 4.0 17.3 1.0
CA A:HIS71 4.0 19.5 1.0
CD2 A:HIS63 4.1 16.6 1.0
NE2 A:HIS71 4.1 17.8 1.0
NE2 A:HIS80 4.1 18.1 1.0
CD2 A:HIS80 4.2 17.1 1.0
CD2 A:HIS71 4.3 17.3 1.0
CB A:ASP83 4.3 19.0 1.0
C A:LYS136 4.7 24.1 1.0
O A:HOH205 4.7 31.4 1.0
CA A:ASP83 4.8 20.1 1.0
CA A:HIS80 4.8 18.2 1.0
N A:HIS80 4.8 18.9 1.0
CA A:HIS63 4.9 14.0 1.0
N A:HIS71 5.0 20.4 1.0
N A:ASP83 5.0 19.6 1.0

Reference:

P.J.Hart, M.M.Balbirnie, N.L.Ogihara, A.M.Nersissian, M.S.Weiss, J.S.Valentine, D.Eisenberg. A Structure-Based Mechanism For Copper-Zinc Superoxide Dismutase. Biochemistry V. 38 2167 1999.
ISSN: ISSN 0006-2960
PubMed: 10026301
DOI: 10.1021/BI982284U
Page generated: Sat Oct 12 22:23:16 2024

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